Regulated CPEB phosphorylation during meiotic progression suggests a mechanism for temporal control of maternal mRNA translation

  1. Joyce Tay1,
  2. Rebecca Hodgman,
  3. Madathia Sarkissian, and
  4. Joel D. Richter2
  1. Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA

Abstract

CPEB is an mRNA-binding protein that stimulates polyadenylation-induced translation of maternal mRNA once it is phosphorylated on Ser 174 or Thr 171 (species-dependent). Disruption of the CPEB gene in mice causes an arrest of oogenesis at embryonic day 16.5 (E16.5), when most oocytes are in pachytene of prophase I. Here, we show that CPEB undergoes Thr 171 phosphorylation at E16.5, but dephosphorylation at the E18.5, when most oocytes are entering diplotene. Although phosphorylation is mediated by the kinase aurora, the dephosphorylation is due to the phosphatase PP1. The temporal control of CPEB phosphorylation suggests a mechanism in which CPE-containing mRNA translation is stimulated at pachytene and metaphase I.

Keywords

Footnotes

  • Corresponding author.

  • ↵1 Present address: Repligen Corporation, 41 Seyon Street, Waltham, MA 02453

  • ↵2 E-MAIL joel.richter{at}umassmed.edu; FAX (508) 856-4289.

  • Article and publication are at http://www.genesdev.org/cgi/doi/10.1101/gad.1071403.

    • Accepted April 22, 2003.
    • Received December 31, 2002.
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  1. doi: 10.1101/gad.1071403 Genes & Dev. 17: 1457-1462 Cold Spring Harbor Laboratory Press

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